Summary for 9ENR
| Entry DOI | 10.2210/pdb9enr/pdb |
| EMDB information | 19842 |
| Descriptor | Vitellogenin, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, [(2R)-3-[oxidanyl-[2-(trimethyl-$l^{4}-azanyl)ethoxy]phosphoryl]oxy-2-propanoyloxy-propyl] propanoate (3 entities in total) |
| Functional Keywords | yolk, lltp, vwd, ctck, lipid binding protein |
| Biological source | Apis cerana (Asiatic honeybee) |
| Total number of polymer chains | 1 |
| Total formula weight | 202586.98 |
| Authors | Montserrat-Canals, M.,Schnelle, K.,Moeller, A.,Cunha, E.,Luecke, H. (deposition date: 2024-03-13, release date: 2025-03-26, Last modification date: 2025-07-16) |
| Primary citation | Montserrat-Canals, M.,Schnelle, K.,Leipart, V.,Halskau, O.,Amdam, G.V.,Moeller, A.,Cunha, E.S.,Luecke, H. Cryo-EM structure of native honey bee vitellogenin. Nat Commun, 16:5736-5736, 2025 Cited by PubMed Abstract: Vitellogenin (Vg) is the main yolk precursor lipoprotein in almost all egg-laying animals. In addition, along its evolutionary history, Vg has developed a range of new functions in different taxa. In the honey bee, Vg has functions related to immunity, antioxidant protection, social behavior and longevity. However, the molecular mechanisms underlying Vg functionalities are still poorly understood. Here, we report the cryo-EM structure of full-length honey bee Vg, one-step purified directly from hemolymph. The structure provides structural insights into the overall domain architecture, including the lipid binding cavity and the previously uncharacterized von Willebrand factor type D domain. A domain of unknown function has been identified as a C-terminal cystine knot domain based on structural homology. Information about post-translational modifications, cleavage products, metal and lipid binding allow an improved understanding of the mechanisms underlying the range of Vg functionalities. The findings have numerous implications for the structure-function relationship of vitellogenins of other species as well as members of the same protein superfamily, which share the same structural elements. PubMed: 40593495DOI: 10.1038/s41467-025-58575-y PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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